Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody

Peter D. Kwong, Richard Wyatt, James Robinson, Raymond W. Sweet, Joseph Sodroski and Wayne A. Hendrickson ()
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Peter D. Kwong: Columbia University
Richard Wyatt: Dana-Farber Cancer Institute, Harvard Medical School, Harvard School of Public Health
James Robinson: Tulane University Medical Center
Raymond W. Sweet: SmithKline Beecham Pharmaceuticals
Joseph Sodroski: Dana-Farber Cancer Institute, Harvard Medical School, Harvard School of Public Health
Wayne A. Hendrickson: Columbia University

Nature, 1998, vol. 393, issue 6686, 648-659

Abstract: Abstract The entry of human immunodeficiency virus (HIV) into cells requires the sequential interaction of the viral exterior envelope glycoprotein, gp120, with the CD4 glycoprotein and a chemokine receptor on the cell surface. These interactions initiate a fusion of the viral and cellular membranes. Although gpl20 can elicit virus-neutralizing antibodies, HIV eludes the immune system. We have solved the X-ray crystal structure at 2.5 Å resolution of an HIV-1 gp120 core complexed with a two-domain fragment of human CD4 and an antigen-binding fragment of a neutralizing antibody that blocks chemokine-receptor binding. The structure reveals a cavity-laden CD4–gp120 interface, a conserved binding site for the chemokine receptor, evidence for a conformational change upon CD4 binding, the nature of a CD4-induced antibody epitope, and specific mechanisms for immune evasion. Our results provide a framework for understanding the complex biology of HIV entry into cells and should guide efforts to intervene.

Date: 1998
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DOI: 10.1038/31405

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